2a93

NMR SOLUTION STRUCTURE OF THE C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER, 40 STRUCTURES

Method: SOLUTION NMR Dmax: 54.8 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER

OrganismNot specified

UniProt P01106

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 406–434 Fragment:LEUCINE ZIPPER Non-standard monomer:Yes (specific site not provided by mmCIF) C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER × 1 (P28574) SOLUTION NMR NMR measurement conditions:pH 4.8;298 K;Ionic strength (raw mmCIF value) 100 mM;Pressure 1 NMR sample composition:WATER Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

18 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–33; UniProt 406–434

C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER

OrganismNot specified

UniProt P28574

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 74–102 Fragment:LEUCINE ZIPPER Non-standard monomer:Yes (specific site not provided by mmCIF) C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER × 1 (P01106) SOLUTION NMR NMR measurement conditions:pH 4.8;298 K;Ionic strength (raw mmCIF value) 100 mM;Pressure 1 NMR sample composition:WATER Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MAX_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–33; UniProt 74–102

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 2a93

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2a93
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2a93
Deposition date deposition_date1998-06-09
Structure title titleNMR SOLUTION STRUCTURE OF THE C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER, 40 STRUCTURES
Keywords keywordsLEUCINE ZIPPERS, 2D NMR, SOLUTION STRUCTURE, H-BONDS, BURIED SALT BRIDGE; LEUCINE ZIPPERS
Experimental Method methodSOLUTION NMR

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.57
Radius of gyration Rg (electron density) rg_electron14.83
Forward intensity I(0) i01532910000.00
Molecular weight molecular_weight305670.0 kDa
Excluded volume excluded_volume373630 ų
Envelope volume envelope_volume24103 ų
Hydration-shell volume shell_volume12626 ų
Envelope diameter envelope_diameter58.7
Shell Rg shell_rg22.08
Envelope Rg envelope_rg17.78
Shape Rg shape_rg14.71
Total Rg total_rg15.27
Total atoms total_atoms43120
Residues n_residues2560
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax54.8
Rg (real space) rg_real15.57
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real1.5480e+09
I(0) uncertainty (real space) i0_real_error1.7830e+07
Rg (reciprocal space) rg_reciprocal14.78
I(0) (reciprocal space) i0_reciprocal1533000000.0000
Solution quality estimate total_estimate0.5582
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary13.2
Skewness Skewness skewness0.650
Kurtosis Kurtosis kurtosis-0.189
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha6.8200
Highest regularization parameter α highest_alpha114000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.585; Stabil: 0.888; Sysdev: 0.000; Positv: 1.000; Valcen: 0.227; Smooth: 0.632

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2a93a1
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.3 — Leucine zipper domain
Family Family familyh.1.3.1 — Leucine zipper domain
Domain ID domain_idd2a93a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2a93b_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.3 — Leucine zipper domain
Family Family familyh.1.3.1 — Leucine zipper domain

8. Citations (1)

9. Files and Curves (10)